Structural Analysis of Type III Collagen Using Two Dimensional Nuclear Magnetic Resonance.

Type III collagen belongs to one of the twenty-eight known collagen types. It is found throughout the body, including being a major component of blood vessels, internal organs, and skin. A collagen molecule comprises of over a thousand amino acids, which are all arranged in three left-handed peptide chains folded together into a characteristic right-handed triple helix. Type III collagen is known to play a role in wound healing and tissue repair, and is the cause for hereditary Ehlers-Danlos syndrome (EDS) type IV which often leads to ruptures of large arteries and internal organs and, in severe cases, death. However, due to the large size of its molecule, not much is known about how type III collagen's structure influences the functions it has in the body. Two-dimensional nuclear magnetic resonance (2D NMR) is a relatively new analytical technique that has become increasingly more utilized in the study of biological molecules, since it has the ability to detect relationships of atoms both through their bonds and through space. Still, because of the length and repetitive nature of its sequence, the best way to study the collagen molecule by NMR is with model peptide sequences that mimic a particular collagen segment of interest. This review summarizes the research conducted up to this point on collagens using nuclear magnetic resonance. [ABSTRACT FROM AUTHOR]